Detection and analysis of (O-linked beta-N-acetylglucosamine)-modified proteins.
Glycosylation is one of the most common and complex forms of posttranslational modifications of proteins in eukaryotes. Seven different protein-carbohydrate linkages have been characterized on nuclear and cytoplasmic glycoproteins, the most widespread of which is the modification of Ser/Thr residues with monosaccharides of O-linked beta-N-acetylglucosamine (O-GlcNAc). O-GlcNAc modification is concentrated in nuclear proteins. O-GlcNAc is thought to regulate protein function in a manner analogous to phosphorylation; and is implicated in the regulation of transcription, the proteasome, insulin and MAP kinase signaling, the cell cycle, and the cellular stress response. In this chapter we focus on methods for the detection of O-GlcNAc-modified proteins and discuss general techniques for the detection and subsequent analysis of other protein-carbohydrate conjugates.
Zachara
Natasha E
NE
The Department of Biological Chemistry, The Johns Hopkins University School of Medicine, Baltimore, MD, USA.
D000117:Acetylglucosamine / Q000737:chemistry* / Q000378:metabolism*; D000818:Animals; D002478:Cells, Cultured; D002846:Chromatography, Affinity; D006031:Glycosylation; D006801:Humans; D013058:Mass Spectrometry; D011506:Proteins / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*
D011506:Proteins; D000117:Acetylglucosamine